Evidence map›Paper›PMID 40214427›Full record

ReviewCells2025

Decoding Plant Ribosomal Proteins: Multitasking Players in Cellular Games.

Dariusz Stępiński

Abstract readReview
In one paragraph

Review in Cells, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Dariusz StępińskiDepartment of Cytophysiology, Institute of Experimental Biology, Faculty of Biology and Environmental Protection, University of Lodz, Pomorska 141/143, 90-236 Lodz, Poland.ORCID 0000-0002-7232-5686

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosomal proteins (RPs) were traditionally considered as ribosome building blocks, serving exclusively in ribosome assembly. However, contemporary research highlights their involvement in additional translational roles, as well as diverse non-ribosomal activities. The functional diversity of RPs is further enriched by the presence of 2-7 paralogs per RP family in plants, suggesting that these proteins may perform distinct, specialized functions. The spatiotemporal expression of RP paralogs allows for the assembly of unique ribosomes (ribosome heterogeneity), enabling the selective translation of specific mRNAs, and producing specialized proteins essential for plant functioning. Additionally, RPs that operate independently of ribosomes as free molecules may regulate a wide range of physiological processes. RPs involved in protein biosynthesis within the cytosol, mitochondria, or plastids are encoded by distinct genes, which account for their functional specialization. Notably, RPs associated with plastid or mitochondrial ribosomes, beyond their canonical roles in these organelles, also contribute to overall plant development and functionality, akin to their cytosolic counterparts. This review explores the roles of RPs in different cellular compartments, the presumed molecular mechanisms underlying their functions, and the involvement of other molecular factors that cooperate with RPs in these processes. In addition to the new RP nomenclature introduced in 2022/2023, the old names are also applied.

Indexed as

Plant ProteinsPlantsRibosomal ProteinsMitochondriaPlastidsProtein BiosynthesisRibosomesPlant ProteinsRibosomal Proteinsplant cellular ribosomal proteinsplant developmentribosomal protein paralogsribosome heterogeneitystress response

Identifiers

PMID40214427
PMCPMC11987935

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.